ID   ELP4_DANRE              Reviewed;         397 AA.
AC   Q566Y1; A2BDL9;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 2.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Elongator complex protein 4;
DE            Short=ELP4;
GN   Name=elp4; ORFNames=si:dkey-157g7.1, zgc:112389;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the elongator complex which is required for
CC       multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl
CC       uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U
CC       (5-carbamoylmethyl uridine). The elongator complex catalyzes the
CC       formation of carboxymethyluridine in the wobble base at position 34 in
CC       tRNAs. {ECO:0000250|UniProtKB:Q96EB1}.
CC   -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC       biosynthesis. {ECO:0000250|UniProtKB:Q96EB1}.
CC   -!- SUBUNIT: Component of the elongator complex.
CC       {ECO:0000250|UniProtKB:Q96EB1}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96EB1}. Nucleus
CC       {ECO:0000250|UniProtKB:Q96EB1}.
CC   -!- SIMILARITY: Belongs to the ELP4 family. {ECO:0000305}.
CC   -!- CAUTION: The elongator complex was originally thought to play a role in
CC       transcription elongation. However, it is no longer thought to play a
CC       direct role in this process and its primary function is thought to be
CC       in tRNA modification. {ECO:0000250|UniProtKB:Q96EB1}.
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DR   EMBL; BX000453; CAM15102.1; -; Genomic_DNA.
DR   EMBL; CT030217; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC093280; AAH93280.1; -; mRNA.
DR   RefSeq; NP_001017638.1; NM_001017638.1.
DR   AlphaFoldDB; Q566Y1; -.
DR   SMR; Q566Y1; -.
DR   STRING; 7955.ENSDARP00000015880; -.
DR   PaxDb; Q566Y1; -.
DR   Ensembl; ENSDART00000002498; ENSDARP00000015880; ENSDARG00000008852.
DR   GeneID; 550331; -.
DR   KEGG; dre:550331; -.
DR   CTD; 26610; -.
DR   ZFIN; ZDB-GENE-050417-114; elp4.
DR   eggNOG; KOG3949; Eukaryota.
DR   GeneTree; ENSGT00390000001443; -.
DR   HOGENOM; CLU_031345_3_0_1; -.
DR   InParanoid; Q566Y1; -.
DR   OMA; NTTMWDD; -.
DR   PhylomeDB; Q566Y1; -.
DR   TreeFam; TF320797; -.
DR   UniPathway; UPA00988; -.
DR   PRO; PR:Q566Y1; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 7.
DR   Bgee; ENSDARG00000008852; Expressed in mature ovarian follicle and 20 other tissues.
DR   ExpressionAtlas; Q566Y1; baseline.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0033588; C:elongator holoenzyme complex; IBA:GO_Central.
DR   GO; GO:0008023; C:transcription elongation factor complex; ISS:UniProtKB.
DR   GO; GO:0008607; F:phosphorylase kinase regulator activity; ISS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0002098; P:tRNA wobble uridine modification; IBA:GO_Central.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR008728; Elongator_complex_protein_4.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR12896; PTHR12896; 1.
DR   Pfam; PF05625; PAXNEB; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Nucleus; Reference proteome; tRNA processing.
FT   CHAIN           1..397
FT                   /note="Elongator complex protein 4"
FT                   /id="PRO_0000284006"
FT   CONFLICT        30
FT                   /note="F -> S (in Ref. 2; AAH93280)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        47
FT                   /note="S -> P (in Ref. 2; AAH93280)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        331
FT                   /note="R -> L (in Ref. 2; AAH93280)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   397 AA;  43752 MW;  11FDF70FB5FB9957 CRC64;
     MAAPVRGMAV SSSIGNTTSF QKKTRSKLVF IPGTRPSVQN GQLLVSSGVS SLDYVIGGGL
     AVGTLLLVEE DRYDSYSRML LKYFLAEGIV CGHELFLASA RDHPDQIMQE LPSPILDDVA
     SMKMSEGQSQ PNDPDNPDTM KIAWRYQNQP RVQTALASSS RFGHYYDASK TMDPELLQAA
     KYHSFYQLQE TPVTTGLSSL PSPYLALLKS IQTLIQKEGF DGSTPQLRGR NVLRVGLHSL
     GSVLWGDDVC CKDNSAHCHA LSTFLYALRG LLRTSLSVAM MTVPSHLIQS RAVMGRIIRL
     SDTAIALESF RGSEKETNPL YKDYHGLLYV RQIPRLNCLT SEVPDTKDLA FKLKRKQFTI
     ERLHLPPDLS ETVSRVSKAD LAAGCASTAT GNKHLHF